First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in non-heme Fe enzymes

被引：9

作者：

Light, Kenneth M. ^{[1
]}

Hangasky, John A. ^{[2
]}

Knapp, Michael J. ^{[2
]}

Solomon, Edward I. ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

[2] Univ Massachusetts, Dept Chem, Amherst, MA 01003 USA

来源：

DALTON TRANSACTIONS | 2014年 / 43卷 / 04期

关键词：

KG-DEPENDENT OXYGENASES; O-2; ACTIVATION; PHENYLALANINE-HYDROXYLASE; CRYSTAL-STRUCTURE; IRON; DIOXYGENASE; MECHANISM; SYNTHASE; BIOSYNTHESIS; CHEMISTRY;

D O I：

10.1039/c3dt53201a

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Non-heme Fe(II) enzymes exhibit a general mechanistic strategy where binding all cosubstrates opens a coordination site on the Fe(II) for O-2 activation. This study shows that strong-donor ligands, steric interactions with the substrate and second-sphere H-bonding to the facial triad carboxylate allow for five-coordinate site formation in this enzyme superfamily.

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页码：1505 / 1508

页数：4

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